Human ATM Antibody

ATM (Ataxia Telangiectasia Mutated) is a 350-370 kDa member of the ATM subfamily, PI3/PI4-kinase family of enzymes. It is ubiquitously expressed, and serves as a DNA damage sensor. ATM is activated via autophosphorylation at double strand breaks. Following activation, multiple substrates are phosphorylated, including Chk2, and ATR is recruited and activated as part of an integrated repair circuit. Human ATM is 3056 amino acids (aa) in length. It contains one FAT (focal adhesion targeting) domain (aa 1960-2566), a PI‑3/PI‑4 kinase catalytic domain (aa 2712-2962) and a second, C-terminal FAT domain (aa 3024-3056). There are at least six Ser and four Thr utilized phosphorylation sites, and one critical acetylation activation site at Lys3016. There are at least four potential splice variants. One shows a Trp substitution for aa 536-3056, a second contains an eight aa substitution for aa 2506-3056, a third possesses a five aa substitution for aa 1637-3056, while a fourth contains a premature truncation after Lys2756. Over aa 2138-2400, human ATM shares 82% aa identity with mouse ATM.